Reactive oxygen and nitrogen species are currently considered not only harmful byproducts of aerobic respiration but also critical mediators of redox signaling. The molecules and the chemical principles sustaining the network of cellular redox regulated processes are described. Special emphasis is placed on hydrogen peroxide (H2O2), now considered as acting as a second messenger, and on sulfhydryl groups, which are the direct targets of the oxidant signal. Cysteine residues of some proteins, therefore, act as sensors of redox conditions and are oxidized in a reversible reaction. In particular, the formation of sulfenic acid and disulfide, the initial steps of thiol oxidation, are described in detail. The many cell pathways involved in reactive oxygen species formation are reported. Central to redox signaling processes are the glutathione and thioredoxin systems controlling H2O2 levels and, hence, the thiol/disulfide balance. Lastly, some of the most important redox-regulated processes involving specific enzymes and organelles are described. The redox signaling area of research is rapidly expanding, and future work will examine new pathways and clarify their importance in cellular pathophysiology. Antioxid. Redox Signal. 18, 1557–1593.
AnestålK, Prast-NielsenS, CenasN, ArnérESJ. Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLoS One, 3:e1846. 2008.
7.
AntunesF, CadenasE. Estimation of H2O2 gradients across biomembranes. FEBS Lett, 475:121–126. 2000.
8.
Appenzeller-HerzogC. Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum. J Cell Sci, 124:847–855. 2011.
9.
ArnérESJ. Focus on mammalian thioredoxin reductases- Important selenoproteins with versatile functions. Biochim Biophys Acta, 1790:495–526. 2009.
10.
ÅslundF, ZhengM, BeckwithJ, StorzG. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A, 96:6161–6165. 1999.
11.
AwasthiYC, YangY, TiwariNK, PatrickB, SharmaA, LiJ, AwasthiS. Regulation of 4-hydroxynonenal-mediated signaling by glutathione S-transferases. Free Radic Biol Med, 37:607–619. 2004.
12.
BackosDS, FranklinCC, ReiganP. The role of glutathione in brain tumor drug resistance. Biochem Pharmacol, 83:1005–1012. 2012.
13.
BaeYS, KangSW, SeoMS, BainesIC, TekleE, ChockPB, RheeSG. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem, 272:217–221. 1997.
14.
BainesCP, KaiserRA, PurcellNH, BlairNS, OsinskaH, HambletonMA, BrunskillEW, SayenMR, GottliebRA, DornGW, RobbinsJ, MolkentinJD. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature, 434:658–662. 2005.
15.
BairdL, Dinkova-KostovaAT. The cytoprotective role of the Keap1-Nrf2 pathway. Arch Toxicol, 85:241–272. 2011.
16.
BánfiB, MolnárG, MaturanaA, StegerK, HegedûsB, DemaurexN, KrauseKH. A Ca2+-activated NADPH oxidase in testis, spleen, and lymph nodes. J Biol Chem, 276:37594–37601. 2001.
17.
BarrettWC, DeGnoreJP, KengYF, ZhangZY, YimMB, ChockPB. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J Biol Chem, 274:34543–34546. 1999.
18.
BarrettWC, DeGnoreJP, KonigS, FalesHM, KengYF, ZhangZY, YimMB, ChockPB. Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry, 38:6699–6705. 1999.
19.
BeckCF. Signaling pathways from the chloroplast to the nucleus. Planta, 222:743–756. 2005.
20.
BedardK, KrauseKH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev, 87:245–313. 2007.
21.
BeerSM, TaylorER, BrownSE, DahmCC, CostaNJ, RunswickMJ, MurphyMP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins. Implications for mitochondrial redox regulation and antioxidant defense. J Biol Chem, 279:47939–47951. 2004.
22.
BellEL, KlimovaTA, EisenbartJ, MoraesCT, MurphyMP, BudingerGRS, ChandelNS. The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. J Cell Biol, 177:1029–1036. 2007.
23.
BenharM, ForresterMT, HessDT, StamlerJS. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science, 320:1050–1054. 2008.
24.
BernardiP. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev, 79:1127–1155. 1999.
25.
BerndtC, LilligCH, HolmgrenA. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol, 292:H1227–H1236. 2007.
26.
Berners-PriceSJ, FilipovskaA. Gold compounds as therapeutic agents for human diseases. Metallomics, 3:863–873. 2011.
27.
BerraE, BenizriE, GinouvesA, VolmatV, RouxD, PouyssegurJ. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J, 22:4082–4090. 2003.
28.
BienertGP, MøllerAL, KristiansenKA, SchulzA, MøllerIM, SchjoerringJK, JahnTP. Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J Biol Chem, 282:1183–1192. 2007.
29.
BienertGP, SchjoerringJK, JahnTP. Membrane transport of hydrogen peroxide. Biochim Biophys Acta, 1758:994–1003. 2006.
30.
BindoliA, CallegaroMT, BarzonE, BenettiM, RigobelloMP. Influence of the redox state of pyridine nucleotides on mitochondrial sulfhydryl groups and permeability transition. Arch Biochem Biophys, 342:22–28. 1997.
31.
BindoliA, CavalliniL, RigobelloMP, CoassinM, Di LisaF. Modification of the xanthine-converting enzyme of perfused rat heart during ischemia and oxidative stress. Free Radic Biol Med, 4:163–167. 1988.
32.
BindoliA, DeebleDJ, RigobelloMP, GalzignaL. Direct and respiratory chain-mediated redox cycling of adrenochrome. Biochim Biophys Acta, 1016:349–356. 1990.
33.
BindoliA, FleischerS. Induced Ca2+ release in skeletal muscle sarcoplasmic reticulum by sulfhydryl reagents and chlorpromazine. Arch Biochem Biophys, 221:458–466. 1983.
34.
BindoliA, FukutoJM, FormanHJ. Thiol chemistry in peroxidase catalysis and redox signaling. Antioxid Redox Signal, 10:1549–1564. 2008.
35.
BindoliA, RigobelloMP, DeebleDJ. Biochemical and toxicological properties of the oxidation products of catecholamines. Free Radic Biol Med, 13:391–405. 1992.
36.
BindoliA, RigobelloMP, ScutariG, GabbianiC, CasiniA, MessoriL. Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs. Coordin Chem Rev, 253:1692–1707. 2009.
37.
BiswasSK, RahmanI. Environmental toxicity, redox signaling and lung inflammation: the role of glutathione. Mol Aspects Med, 30:60–76. 2009.
38.
BiteauB, LabarreJ, ToledanoMB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature, 425:980–984. 2003.
39.
BlockK, GorinY, AbboudHE. Subcellular localization of Nox4 and regulation in diabetes. Proc Natl Acad Sci U S A, 106:14385–14390. 2009.
40.
BloomD, DhakshinamoorthyS, JaiswalAK. Site-directed mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene. Oncogene, 21:2191–2200. 2002.
41.
BragadinM, ScutariG, FoldaA, BindoliA, RigobelloMP. Effect of metal complexes on thioredoxin reductase and the regulation of mitochondrial permeability conditions. Ann N Y Acad Sci, 1030:348–354. 2004.
42.
BrandMD. The sites and topology of mitochondrial superoxide production. Exp Gerontol, 45:466–472. 2010.
Brigelius-FlohéR, BanningA. Part of the series: from dietary antioxidants to regulators in cellular signaling and gene regulation. Sulforaphane and selenium, partners in adaptive response and prevention of cancer. Free Radic Res, 40:775–787. 2006.
45.
Brigelius-FlohéR, FlohéL. Basic principles and emerging concepts in the redox control of transcription factors. Antioxid Redox Signal, 15:2335–2381. 2011.
46.
Brigelius-FlohéR, MüllerM, LippmannD, KippAP. The yin and yang of nrf2-regulated selenoproteins in carcinogenesis. Int J Cell Biol, 2012:486147. 2012.
47.
BrivibaK, KissnerR, KoppenolWH, SiesH. Kinetic study of the reaction of glutathione peroxidase with peroxynitrite. Chem Res Toxicol, 11:1398–1401. 1998.
48.
BroniowskaKA, HoggN. The chemical biology of S-nitrosothiols. Antioxid Redox Signal, 17:969–980. 2012.
49.
BroniowskaKA, KeszlerA, BasuS, Kim-ShapiroDB, HoggN. Cytochrome c-mediated formation of S-nitrosothiol in cells. Biochem J, 442:191–197. 2012.
50.
BrownGC, BorutaiteV. There is no evidence that mitochondria are the main source of reactive oxygen species in mammalian cells. Mitochondrion, 12:1–4. 2012.
51.
BrownKK, CoxAG, HamptonMB. Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin. FEBS Lett, 584:1257–1262. 2010.
CasagrandeS, BonettoV, FratelliM, GianazzaE, EberiniI, MassignanT, SalmonaM, ChangG, HolmgrenA, GhezziP. Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci U S A, 99:9745–9749. 2002.
57.
CashTP, PanY, SimonMC. Reactive oxygen species and cellular oxygen sensing. Free Radic Biol Med, 43:1219–1225. 2007.
58.
CederbaumAI. Cytochrome P450 2E1-dependent oxidant stress and upregulation of anti-oxidant defense in liver cells. J Gastroenterol Hepatol, 21,Suppl 3:S22–S25. 2006.
59.
ChakravarthiS, JessopCE, BulleidNJ. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep, 7:271–275. 2006.
ChenY, CaiJ, JonesDP. Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett, 580:6596–6602. 2006.
63.
ChengQ, SandalovaT, LindqvistY, ArnérESJ. Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1. J Biol Chem, 284:3998–4008. 2009.
64.
ChernyakBV, BernardiP. The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites. Eur J Biochem, 238:623–630. 1996.
65.
ChiarugiP. PTPs versus PTKs: the redox side of the coin. Free Radic Res, 39:353–364. 2005.
66.
ChungYM, KimJS, YooYD. A novel protein, Romo1, induces ROS production in the mitochondria. Biochem Biophys Res Commun, 347:649–655. 2006.
67.
ClaiborneA, MillerH, ParsonageD, RossRP. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J, 7:1483–1490. 1993.
68.
ConnernCP, HalestrapAP. Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem J, 302,Pt 2:321–324. 1994.
69.
ConradM. Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4. Biochim Biophys Acta, 1790:1575–1585. 2009.
70.
ConradM, JakupogluC, MorenoSG, LipplS, BanjacA, SchneiderM, BeckH, HatzopoulosAK, JustU, SinowatzF, SchmahlW, ChienKR, WurstW, BornkammGW, BrielmeierM. Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol Cell Biol, 24:9414–9423. 2004.
71.
ConradM, SandinÅ, ForsterH, SeilerA, FrijhoffJ, DagnellM, BornkammGW, RådmarkO, Hooft van HuijsduijnenR, AspenströmP, BöhmerF, ÖstmanA. 12/15-lipoxygenase-derived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases. Proc Natl Acad Sci U S A, 107:15774–15779. 2010.
CostaVM, CarvalhoF, BastosML, CarvalhoRA, CarvalhoM, RemiãoF. Contribution of catecholamine reactive intermediates and oxidative stress to the pathologic features of heart diseases. Curr Med Chem, 18:2272–2314. 2011.
74.
CostantiniP, BelzacqAS, VieiraHL, LarochetteN, de PabloMA, ZamzamiN, SusinSA, BrennerC, KroemerG. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene, 19:307–314. 2000.
75.
CostantiniP, ChernyakBV, PetronilliV, BernardiP. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J Biol Chem, 271:6746–6751. 1996.
76.
CoxAG, BrownKK, ArnerESJ, HamptonMB. The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation. Biochem Pharmacol, 76:1097–1109. 2008.
77.
CuozzoJW, KaiserCA. Competition between glutathione and protein thiols for disulphide-bond formation. Nat Cell Biol, 1:130–135. 1999.
78.
D'AutréauxB, ToledanoMB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol, 8:813–824. 2007.
79.
DaiberA. Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species. Biochim Biophys Acta, 1797:897–906. 2010.
80.
Dalle-DonneI, ColomboG, GaglianoN, ColomboR, GiustariniD, RossiR, MilzaniA. S-glutathiolation in life and death decisions of the cell. Free Radic Res, 45:3–15. 2011.
81.
Dalle-DonneI, MilzaniA, GaglianoN, ColomboR, GiustariniD, RossiR. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid Redox Signal, 10:445–473. 2008.
82.
DamdimopoulosAE, Miranda-VizueteA, Pelto-HuikkoM, GustafssonJA, SpyrouG. Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death. J Biol Chem, 277:33249–33257. 2002.
83.
DavisFA, JenkinsLA, BillmersRL. Chemistry of sulfenic acids.7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogenbonding and electronegativity effects. J Org Chem, 51:1033–1040. 1986.
84.
De DekenX, WangD, DumontJE, MiotF. Characterization of ThOX proteins as components of the thyroid H2O2-generating system. Exp Cell Res, 273:187–196. 2002.
85.
DelaunayA, PfliegerD, BarraultMB, VinhJ, ToledanoMB. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation. Cell, 111:471–481. 2002.
86.
Della CorteE, StirpeF. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme. Biochem J, 126:739–745. 1972.
87.
DenuJM, TannerKG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry, 37:5633–5642. 1998.
88.
DeYuliaGJJr., CárcamoJM, Bórquez-OjedaO, SheltonCC, GoldeDW. Hydrogen peroxide generated extracellularly by receptor-ligand interaction facilitates cell signaling. Proc Natl Acad Sci U S A, 102:5044–5049. 2005.
DikalovS. Cross talk between mitochondria and NADPH oxidases. Free Radic Biol Med, 51:1289–1301. 2011.
91.
Dinkova-KostovaAT, HoltzclawWD, ColeRN, ItohK, WakabayashiN, KatohY, YamamotoM, TalalayP. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci U S A, 99:11908–11913. 2002.
92.
EllisHR, PooleLB. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry, 36:15013–15018. 1997.
93.
EpsteinACR, GleadleJM, McNeillLA, HewitsonKS, O'RourkeJ, MoleDR, MukherjiM, MetzenE, WilsonMI, DhandaA, TianYM, MassonN, HamiltonDL, JaakkolaP, BarsteadR, HodgkinJ, MaxwellPH, PughCW, SchofieldCJ, RatcliffePJ. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell, 107:43–54. 2001.
94.
EsworthyRS, HoYS, ChuFF. The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch Biochem Biophys, 340:59–63. 1997.
95.
FaccioG, NivalaO, KruusK, BuchertJ, SaloheimoM. Sulfhydryl oxidases: sources, properties, production and applications. Appl Microbiol Biotechnol, 91:957–966. 2011.
96.
FangJ, LuJ, HolmgrenA. Thioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity. J Biol Chem, 280:25284–25290. 2005.
97.
FassD. Hunting for alternative disulfide bond formation pathways: endoplasmic reticulum janitor turns professor and teaches a lesson. Mol Cell, 40:685–686. 2010.
98.
Ferrer-SuetaG, MantaB, BottiH, RadiR, TrujilloM, DenicolaA. Factors affecting protein thiol reactivity and specificity in peroxide reduction. Chem Res Toxicol, 24:434–450. 2011.
99.
Ferrer-SuetaG, RadiR. Chemical biology of peroxynitrite: kinetics, diffusion, and radicals. ACS Chem Biol, 4:161–177. 2009.
FinkelT. Redox-dependent signal transduction. FEBS Lett, 476:52–54. 2000.
104.
FinkelT. Signal transduction by mitochondrial oxidants. J Biol Chem, 287:4434–4440. 2012.
105.
FlohéL. Changing paradigms in thiology from antioxidant defense toward redox regulation. Methods Enzymol, 473:1–39. 2010.
106.
FlohéL, Brigelius-FlohéR, SaliouC, TraberMG, PackerL. Redox regulation of NF-kappa B activation. Free Radic Biol Med, 22:1115–1126. 1997.
107.
FlohéL, ToppoS, CozzaG, UrsiniF. A comparison of thiol peroxidase mechanisms. Antioxid Redox Signal, 15:763–780. 2011.
108.
FormanHJ. Use and abuse of exogenous H2O2 in studies of signal transduction. Free Radic Biol Med, 42:926–932. 2007.
109.
FormanHJ, FridovichI. Superoxide dismutase: a comparison of rate constants. Arch Biochem Biophys, 158:396–400. 1973.
110.
FormanHJ, FukutoJM, MillerT, ZhangH, RinnaA, LevyS. The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal. Arch Biochem Biophys, 477:183–195. 2008.
111.
FormanHJ, FukutoJM, TorresM. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol, 287:C246–C256. 2004.
112.
FormanHJ, KennedyJA. Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem Biophys Res Commun, 60:1044–1050. 1974.
FosterDB, Van EykJE, MarbánE, O'RourkeB. Redox signaling and protein phosphorylation in mitochondria: progress and prospects. J Bioenerg Biomembr, 41:159–168. 2009.
115.
FourquetS, GueroisR, BiardD, ToledanoMB. Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation. J Biol Chem, 285:8463–8471. 2010.
116.
FourquetS, HuangME, D'AutreauxB, ToledanoMB. The dual functions of thiol-based peroxidases in H2O2 scavenging and signaling. Antioxid Redox Signal, 10:1565–1576. 2008.
117.
FragaCG, OteizaPI. Dietary flavonoids: Role of (-)-epicatechin and related procyanidins in cell signaling. Free Radic Biol Med, 51:813–823. 2011.
118.
FransenM, NordgrenM, WangB, ApanasetsO. Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease. Biochim Biophys Acta, 1822:1363–1373. 2012.
119.
FratelliM, DemolH, PuypeM, CasagrandeS, VillaP, EberiniI, VandekerckhoveJ, GianazzaE, GhezziP. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics, 3:1154–1161. 2003.
120.
FridovichI. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J Biol Chem, 245:4053–4057. 1970.
121.
FridovichI. The biology of oxygen radicals. Science, 201:875–880. 1978.
122.
FriesenC, KiessY, DebatinKM. A critical role of glutathione in determining apoptosis sensitivity and resistance in leukemia cells. Cell Death Differ, 11,Suppl 1:S73–S85. 2004.
123.
FujimotoM, HayashiT. New insights into the role of mitochondria-associated endoplasmic reticulum membrane. Int Rev Cell Mol Biol, 292:73–117. 2011.
124.
GeisztM, LetoTL. The Nox family of NAD(P)H oxidases: host defense and beyond. J Biol Chem, 279:51715–51718. 2004.
125.
GertzM, SteegbornC. The lifespan-regulator p66Shc in mitochondria: redox enzyme or redox sensor?Antioxid Redox Signal, 13:1417–1428. 2010.
126.
GiannoniE, BuricchiF, RaugeiG, RamponiG, ChiarugiP. Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol Cell Biol, 25:6391–6403. 2005.
127.
GiorgioM, MigliaccioE, OrsiniF, PaolucciD, MoroniM, ContursiC, PellicciaG, LuziL, MinucciS, MarcaccioM, PintonP, RizzutoR, BernardiP, PaolucciF, PelicciPG. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell, 122:221–233. 2005.
128.
GiorgioM, TrineiM, MigliaccioE, PelicciPG. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals?Nat Rev Mol Cell Biol, 8:722–728. 2007.
129.
GirottiAW. Translocation as a means of disseminating lipid hydroperoxide-induced oxidative damage and effector action. Free Radic Biol Med, 44:956–968. 2008.
130.
GirottiAW, KriskaT. Role of lipid hydroperoxides in photo-oxidative stress signaling. Antioxid Redox Signal, 6:301–310. 2004.
131.
GitlerC, ZarmiB, KalefE, MellerR, ZorU, GoldmanR. Calcium-dependent oxidation of thioredoxin during cellular growth initiation. Biochem Biophys Res Commun, 290:624–628. 2002.
132.
GloireG, Legrand-PoelsS, PietteJ. NF-κB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol, 72:1493–1505. 2006.
GoYM, JonesDP. Redox control systems in the nucleus: mechanisms and functions. Antioxid Redox Signal, 13:489–509. 2010.
135.
GoossensV, De VosK, VercammenD, SteemansM, VancompernolleK, FiersW, VandenabeeleP, GrootenJ. Redox regulation of TNF signaling. Biofactors, 10:145–156. 1999.
136.
GotoK, HollerM, OkazakiR. Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent: the first synthesis of a stable sulfenic acid by direct oxidation of a thiol. J Am Chem Soc, 119:1460–1461. 1997.
137.
GowAJ, BuerkDG, IschiropoulosH. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem, 272:2841–2845. 1997.
138.
GrahamKA, KulawiecM, OwensKM, LiX, DesoukiMM, ChandraD, SinghKK. NADPH oxidase 4 is an oncoprotein localized to mitochondria. Cancer Biol Ther, 10:223–231. 2010.
139.
GromerS, ArscottLD, WilliamsCHJr., SchirmerRH, BeckerK. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem, 273:20096–20101. 1998.
140.
GromerS, UrigS, BeckerK. The thioredoxin system-From science to clinic. Med Res Rev, 24:40–89. 2004.
141.
GuengerichFP. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol, 14:611–650. 2001.
HalestrapAP. What is the mitochondrial permeability transition pore?J Mol Cell Cardiol, 46:821–831. 2009.
144.
HalestrapAP, DavidsonAM. Inhibition of Ca2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem J, 268:153–160. 1990.
145.
HallA, ParsonageD, PooleLB, KarplusPA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J Mol Biol, 402:194–209. 2010.
146.
HalliwellB, GutteridgeJMC. Free Radicals in Biology and Medicine. New York: Oxford University Press, 2007; 851.
HanschmannEM, LonnME, SchutteLD, FunkeM, GodoyJR, EitnerS, HudemannC, LilligCH. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. J Biol Chem, 285:40699–40705. 2010.
149.
HansenJM, WatsonWH, JonesDP. Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol Sci, 82:308–317. 2004.
150.
HansenJM, ZhangH, JonesDP. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med, 40:138–145. 2006.
151.
HansenJM, ZhangH, JonesDP. Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-α-induced reactive oxygen species generation, NF-κB activation, and apoptosis. Toxicol Sci, 91:643–650. 2006.
152.
HatahetF, RuddockLW. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal, 11:2807–2850. 2009.
153.
HawkinsBJ, MadeshM, KirkpatrickCJ, FisherAB. Superoxide flux in endothelial cells via the chloride channel-3 mediates intracellular signaling. Mol Biol Cell, 18:2002–2012. 2007.
154.
HeM, CaiJ, GoYM, JohnsonJM, MartinWD, HansenJM, JonesDP. Identification of thioredoxin-2 as a regulator of the mitochondrial permeability transition. Toxicol Sci, 105:44–50. 2008.
155.
HellK. The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria. Biochim Biophys Acta, 1783:601–609. 2008.
156.
HessDT, MatsumotoA, KimSO, MarshallHE, StamlerJS. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol, 6:150–166. 2005.
157.
HickeyJL, RuhayelRA, BarnardPJ, BakerMV, Berners-PriceSJ, FilipovskaA. Mitochondria-targeted chemotherapeutics: the rational design of gold(I) N-heterocyclic carbene complexes that are selectively toxic to cancer cells and target protein selenols in preference to thiols. J Am Chem Soc, 130:12570–12571. 2008.
158.
HidalgoC, DonosoP. Crosstalk between calcium and redox signaling: from molecular mechanisms to health implications. Antioxid Redox Signal, 10:1275–1312. 2008.
159.
HidalgoC, DonosoP. Cell signaling. Getting to the heart of mechanotransduction. Science, 333:1388–1390. 2011.
160.
HillKE, McCollumGW, BoeglinME, BurkRF. Thioredoxin reductase activity is decreased by selenium deficiency. Biochem Biophys Res Commun, 234:293–295. 1997.
161.
HirotaK, MatsuiM, IwataS, NishiyamaA, MoriK, YodoiJ. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci U S A, 94:3633–3638. 1997.
HoffstromBG, KaplanA, LetsoR, SchmidRS, TurmelGJ, LoDC, StockwellBR. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat Chem Biol, 6:900–906. 2010.
164.
HoggDR. Chemistry of sulphenic acids and esters. The Chemistry of Sulphenic Acids and Their Derivatives. PataiS. New York: John Wiley and Sons, 1990; 361–402.
165.
HollandR, FishbeinJC. Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1. Antioxid Redox Signal, 13:1749–1761. 2010.
166.
HolmgrenA. Thioredoxin. Annu Rev Biochem, 54:237–271. 1985.
167.
HolmgrenA, LuJ. Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem Biophys Res Commun, 396:120–124. 2010.
168.
HolmgrenA, LuthmanM. Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry, 17:4071–4077. 1978.
169.
HwangC, SinskeyAJ, LodishHF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257:1496–1502. 1992.
170.
IñarreaP, MoiniH, HanD, RettoriD, AguilóI, AlavaMA, IturraldeM, CadenasE. Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu, Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis. Biochem J, 405:173–179. 2007.
IshiiT, MoriT, TanakaT, MizunoD, YamajiR, KumazawaS, NakayamaT, AkagawaM. Covalent modification of proteins by green tea polyphenol (-)-epigallocatechin-3-gallate through autoxidation. Free Radic Biol Med, 45:1384–1394. 2008.
173.
IsogaiY, IizukaT, ShiroY. The mechanism of electron donation to molecular oxygen by phagocytic cytochrome b558. J Biol Chem, 270:7853–7857. 1995.
174.
IvashchenkoO, Van VeldhovenPP, BreesC, HoYS, TerleckySR, FransenM. Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk. Mol Biol Cell, 22:1440–1451. 2011.
175.
JacobC, KnightI, WinyardPG. Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways. Biol Chem, 387:1385–1397. 2006.
176.
JakupogluC, PrzemeckGKH, SchneiderM, MorenoSG, MayrN, HatzopoulosAK, de AngelisMH, WurstW, BornkammGW, BrielmeierM, ConradM. Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development. Mol Cell Biol, 25:1980–1988. 2005.
177.
JäschkeA, MiH, TropschugM. Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity. J Mol Biol, 277:763–769. 1998.
178.
JeongW, JungY, KimH, ParkSJ, RheeSG. Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: Implication in the redox regulation of TNF-α signaling. Free Radic Biol Med, 47:1294–1303. 2009.
179.
JeongW, ParkSJ, ChangTS, LeeDY, RheeSG. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J Biol Chem, 281:14400–14407. 2006.
180.
JewettSL, EddyLJ, HochsteinP. Is the autoxidation of catecholamines involved in ischemia-reperfusion injury?Free Radic Biol Med, 6:185–188. 1989.
181.
JocelynPC. Biochemistry of the SH Group; the Occurrence, Chemical Properties, Metabolism and Biological Function of Thiols and Disulphides. London, NY: Academic Press, 1972; 404.
182.
JohanssonC, LilligCH, HolmgrenA. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem, 279:7537–7543. 2004.
JosephSK, NakaoSK, SukumvanichS. Reactivity of free thiol groups in type-I inositol trisphosphate receptors. Biochem J, 393:575–582. 2006.
185.
KabeY, AndoK, HiraoS, YoshidaM, HandaH. Redox regulation of NF-κB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal, 7:395–403. 2005.
186.
KaludercicN, CarpiA, MenabòR, Di LisaF, PaolocciN. Monoamine oxidases (MAO) in the pathogenesis of heart failure and ischemia/reperfusion injury. Biochim Biophys Acta, 1813:1323–1332. 2011.
187.
KelleyEE, KhooNKH, HundleyNJ, MalikUZ, FreemanBA, TarpeyMM. Hydrogen peroxide is the major oxidant product of xanthine oxidase. Free Radic Biol Med, 48:493–498. 2010.
188.
KenslerTW, WakabayashiN. Nrf2: friend or foe for chemoprevention?Carcinogenesis, 31:90–99. 2010.
189.
KenslerTW, WakabayashiN, BiswalS. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol, 47:89–116. 2007.
190.
KettenhofenNJ, WoodMJ. Formation, reactivity, and detection of protein sulfenic acids. Chem Res Toxicol, 23:1633–1646. 2010.
191.
KiceJL. Mechanisms and reactivity in reactions of organic oxyacids of sulfur and their anhydrides. Avances in Physical Organic Chemistry, 17GoldV, BethellD. London: Academic Press, 1980; 65–181.
192.
KileyPJ, BeinertH. The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol, 6:181–185. 2003.
193.
KimJJ, LeeSB, ParkJK, YooYD. TNF-α-induced ROS production triggering apoptosis is directly linked to Romo1 and Bcl-XL. Cell Death Differ, 17:1420–1434. 2010.
194.
KimSO, MerchantK, NudelmanR, BeyerWFJr., KengT, DeAngeloJ, HausladenA, StamlerJS. OxyR: a molecular code for redox-related signaling. Cell, 109:383–396. 2002.
195.
KlotzLO, KrönckeKD, SiesH. Singlet oxygen-induced signaling effects in mammalian cells. Photochem Photobiol Sci, 2:88–94. 2003.
196.
KnockGA, WardJP. Redox regulation of protein kinases as a modulator of vascular function. Antioxid Redox Signal, 15:1531–1547. 2011.
197.
KodaliVK, ThorpeC. Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal, 13:1217–1230. 2010.
KukrejaRC, KontosHA, HessML, EllisEF. PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH. Circ Res, 59:612–619. 1986.
200.
KunduJK, SurhYJ. Nrf2-Keap1 signaling as a potential target for chemoprevention of inflammation-associated carcinogenesis. Pharm Res, 27:999–1013. 2010.
201.
LambethJD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol, 4:181–189. 2004.
202.
LambethJD, KawaharaT, DieboldB. Regulation of Nox and Duox enzymatic activity and expression. Free Radic Biol Med, 43:319–331. 2007.
203.
LandmesserU, DikalovS, PriceSR, McCannL, FukaiT, HollandSM, MitchWE, HarrisonDG. Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension. J Clin Invest, 111:1201–1209. 2003.
LilligCH, HolmgrenA. Thioredoxin and related molecules-From biology to health and disease. Antioxid Redox Signal, 9:25–47. 2007.
212.
LimMD, LorkovicIM, FordPC. NO and NOx interactions with group 8 metalloporphyrins. J Inorg Biochem, 99:151–165. 2005.
213.
LinardD, KandlbinderA, DegandH, MorsommeP, DietzKJ, KnoopsB. Redox characterization of human cyclophilin D: identification of a new mammalian mitochondrial redox sensor?Arch Biochem Biophys, 491:39–45. 2009.
214.
LinnewielK, ErnstH, Caris-VeyratC, Ben-DorA, KampfA, SalmanH, DanilenkoM, LevyJ, SharoniY. Structure activity relationship of carotenoid derivatives in activation of the electrophile/antioxidant response element transcription system. Free Radic Biol Med, 47:659–667. 2009.
215.
LittleC, O'BrienPJ. Mechanism of peroxide-inactivation of the sulphydryl enzyme glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem, 10:533–538. 1969.
216.
LiuH, ZhangH, IlesKE, RinnaA, MerrillG, YodoiJ, TorresM, FormanHJ. The ADP-stimulated NADPH oxidase activates the ASK-1/MKK4/JNK pathway in alveolar macrophages. Free Radic Res, 40:865–874. 2006.
217.
LiuL, HausladenA, ZengM, QueL, HeitmanJ, StamlerJS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature, 410:490–494. 2001.
218.
LohseDL, DenuJM, SantoroN, DixonJE. Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry, 36:4568–4575. 1997.
219.
LoschenG, AzziA, RichterC, FlohéL. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett, 42:68–72. 1974.
220.
LuJ, ChewEH, HolmgrenA. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc Natl Acad Sci U S A, 104:12288–12293. 2007.
221.
LundströmJ, KrauseG, HolmgrenA. A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease. J Biol Chem, 267:9047–9052. 1992.
222.
MaX, ZhangJ, LiuS, HuangY, ChenB, WangD. Nrf2 knockdown by shRNA inhibits tumor growth and increases efficacy of chemotherapy in cervical cancer. Cancer Chemother Pharmacol, 69:485–494. 2012.
223.
MaejimaY, KurodaJ, MatsushimaS, AgoT, SadoshimaJ. Regulation of myocardial growth and death by NADPH oxidase. J Mol Cell Cardiol, 50:408–416. 2011.
224.
MahadevK, WuX, ZilberingA, ZhuL, LawrenceJTR, GoldsteinBJ. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J Biol Chem, 276:48662–48669. 2001.
225.
MaiorinoM, RoveriA, BenazziL, BoselloV, MauriP, ToppoS, TosattoSC, UrsiniF. Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J Biol Chem, 280:38395–38402. 2005.
226.
Mairet-CoelloG, TuryA, Esnard-FeveA, FellmannD, RisoldPY, GriffondB. FAD-linked sulfhydryl oxidase QSOX: topographic, cellular, and subcellular immunolocalization in adult rat central nervous system. J Comp Neurol, 473:334–363. 2004.
227.
MakinoY, YoshikawaN, OkamotoK, HirotaK, YodoiJ, MakinoI, TanakaH. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J Biol Chem, 274:3182–3188. 1999.
228.
MalinouskiM, ZhouY, BelousovVV, HatfieldDL, GladyshevVN. Hydrogen peroxide probes directed to different cellular compartments. PLoS One, 6:e14564. 2011.
229.
MandalPK, SchneiderM, KölleP, KuhlencordtP, FörsterH, BeckH, BornkammGW, ConradM. Loss of thioredoxin reductase 1 renders tumors highly susceptible to pharmacologic glutathione deprivation. Cancer Res, 70:9505–9514. 2010.
230.
ManevichY, FeinsteinSI, FisherAB. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST. Proc Natl Acad Sci U S A, 101:3780–3785. 2004.
231.
MarengoJJ, HidalgoC, BullR. Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells. Biophys J, 74:1263–1277. 1998.
232.
MartindaleJL, HolbrookNJ. Cellular response to oxidative stress: signaling for suicide and survival. J Cell Physiol, 192:1–15. 2002.
233.
MatsuiM, OshimaM, OshimaH, TakakuK, MaruyamaT, YodoiJ, TaketoMM. Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev Biol, 178:179–185. 1996.
234.
MatthewsJR, WakasugiN, VirelizierJL, YodoiJ, HayRT. Thioredoxin regulates the DNA binding activity of NF-κB by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res, 20:3821–3830. 1992.
235.
McIlwainCC, TownsendDM, TewKD. Glutathione S-transferase polymorphisms: cancer incidence and therapy. Oncogene, 25:1639–1648. 2006.
236.
McMahonM, ThomasN, ItohK, YamamotoM, HayesJD. Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a “tethering” mechanism: a two-site interaction model for the Nrf2-Keap1 complex. J Biol Chem, 281:24756–24768. 2006.
237.
McNallyJS, DavisME, GiddensDP, SahaA, HwangJ, DikalovS, JoH, HarrisonDG. Role of xanthine oxidoreductase and NAD(P)H oxidase in endothelial superoxide production in response to oscillatory shear stress. Am J Physiol Heart Circ Physiol, 285:H2290–H2297. 2003.
238.
McStayGP, ClarkeSJ, HalestrapAP. Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore. Biochem J, 367:541–548. 2002.
239.
MeierB, RadekeHH, SelleS, YounesM, SiesH, ReschK, HabermehlGG. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-αBiochem J, 263:539–545. 1989.
240.
MeseckeN, TerziyskaN, KozanyC, BaumannF, NeupertW, HellK, HerrmannJM. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell, 121:1059–1069. 2005.
241.
MieyalJJ, GalloglyMM, QanungoS, SabensEA, SheltonMD. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal, 10:1941–1988. 2008.
242.
MorelY, BaroukiR. Repression of gene expression by oxidative stress. Biochem J, 342,Pt 3:481–496. 1999.
243.
MorganBA, VealEA. Functions of typical 2-Cys peroxiredoxins in yeast. Subcell Biochem, 44:253–265. 2007.
244.
MotohashiK, KoyamaF, NakanishiY, Ueoka-NakanishiH, HisaboriT. Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity. J Biol Chem, 278:31848–31852. 2003.
245.
MurphyMP. How mitochondria produce reactive oxygen species. Biochem J, 417:1–13. 2009.
246.
NaHK, SurhYJ. Modulation of Nrf2-mediated antioxidant and detoxifying enzyme induction by the green tea polyphenol EGCG. Food Chem Toxicol, 46:1271–1278. 2008.
247.
NagyP, KartonA, BetzA, PeskinAV, PaceP, O'ReillyRJ, HamptonMB, RadomL, WinterbournCC. Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study. J Biol Chem, 286:18048–18055. 2011.
248.
NakagawaT, ShimizuS, WatanabeT, YamaguchiO, OtsuK, YamagataH, InoharaH, KuboT, TsujimotoY. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature, 434:652–658. 2005.
249.
NakamuraT, LiptonSA. Emerging role of protein-protein transnitrosylation in cell signaling pathways. Antioxid Redox Signal, 18:239–249. 2013.
250.
NakashimaI, TakedaK, KawamotoY, OkunoY, KatoM, SuzukiH. Redox control of catalytic activities of membrane-associated protein tyrosine kinases. Arch Biochem Biophys, 434:3–10. 2005.
251.
NauserT, KoppenolWH. The rate constant of the reaction of superoxide with nitrogen monoxide: Approaching the diffusion limit. J Phys Chem A, 106:4084–4086. 2002.
252.
NguyenTT, StevensMV, KohrM, SteenbergenC, SackMN, MurphyE. Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore. J Biol Chem, 286:40184–40192. 2011.
253.
NieC, TianC, ZhaoL, PetitPX, MehrpourM, ChenQ. Cysteine 62 of Bax is critical for its conformational activation and its proapoptotic activity in response to H2O2-induced apoptosis. J Biol Chem, 283:15359–15369. 2008.
254.
NiecknigH, TugS, ReyesBD, KirschM, FandreyJ, Berchner-PfannschmidtU. Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia. Free Radic Res, 46:705–717. 2012.
255.
NishiT, ShimizuN, HiramotoM, SatoI, YamaguchiY, HasegawaM, AizawaS, TanakaH, KataokaK, WatanabeH, HandaH. Spatial redox regulation of a critical cysteine residue of NF-κB in vivo. J Biol Chem, 277:44548–44556. 2002.
256.
NishinoT, OkamotoK, EgerBT, PaiEF, NishinoT. Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J, 275:3278–3289. 2008.
257.
NonnL, WilliamsRR, EricksonRP, PowisG. The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol Cell Biol, 23:916–922. 2003.
258.
Okado-MatsumotoA, FridovichI. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. J Biol Chem, 276:38388–38393. 2001.
ParkSJ, KimIS. The role of p38 MAPK activation in auranofin-induced apoptosis of human promyelocytic leukaemia HL-60 cells. Br J Pharmacol, 146:506–513. 2005.
261.
ParsonageD, KarplusPA, PooleLB. Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc Natl Acad Sci U S A, 105:8209–8214. 2008.
262.
PascalI, TarbellDS. The kinetics of the oxidation of a mercaptan to the corresponding disulfide by aqueous hydrogen peroxide. J Am Chem Soc, 79:6015–6020. 1957.
263.
PatwariP, LeeRT. Thioredoxins, mitochondria, and hypertension. Am J Pathol, 170:805–808. 2007.
PeshenkoIV, ShichiH. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Free Radic Biol Med, 31:292–303. 2001.
266.
PeskinAV, LowFM, PatonLN, MaghzalGJ, HamptonMB, WinterbournCC. The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents. J Biol Chem, 282:11885–11892. 2007.
267.
PeskinAV, WinterbournCC. Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radic Biol Med, 30:572–579. 2001.
268.
PiantadosiCA. Regulation of mitochondrial processes by protein S-nitrosylation. Biochim Biophys Acta, 1820:712–721. 2012.
269.
PigietVP, SchusterBJ. Thioredoxin-catalyzed refolding of disulfide-containing proteins. Proc Natl Acad Sci U S A, 83:7643–7647. 1986.
270.
PomposielloPJ, DempleB. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol, 19:109–114. 2001.
271.
PooleLB, ClaiborneA. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J Biol Chem, 264:12330–12338. 1989.
272.
PooleLB, KarplusPA, ClaiborneA. Protein sulfenic acids in redox signaling. Annu Rev Pharmacol Toxicol, 44:325–347. 2004.
273.
PowisG, MontfortWR. Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol, 41:261–295. 2001.
274.
PowisG, MustacichD, CoonA. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med, 29:312–322. 2000.
275.
PriggeJR, ErikssonS, IversonSV, MeadeTA, CapecchiMR, ArnérESJ, SchmidtEE. Hepatocyte DNA replication in growing liver requires either glutathione or a single allele of txnrd1. Free Radic Biol Med, 52:803–810. 2012.
PrützWA. Interactions of hypochlorous acid with pyrimidine nucleotides, and secondary reactions of chlorinated pyrimidines with GSH, NADH, and other substrates. Arch Biochem Biophys, 349:183–191. 1998.
278.
Pushpa-RekhaTR, BurdsallAL, OleksaLM, ChisolmGM, DriscollDM. Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J Biol Chem, 270:26993–26999. 1995.
279.
QuijanoC, AlvarezB, GattiRM, AugustoO, RadiR. Pathways of peroxynitrite oxidation of thiol groups. Biochem J, 322,Pt 1:167–173. 1997.
280.
Quillet-MaryA, JaffrézouJP, MansatV, BordierC, NavalJ, LaurentG. Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J Biol Chem, 272:21388–21395. 1997.
281.
RackhamO, NicholsSJ, LeedmanPJ, Berners-PriceSJ, FilipovskaA. A gold(I) phosphine complex selectively induces apoptosis in breast cancer cells: Implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol, 74:992–1002. 2007.
282.
RadiR, BeckmanJS, BushKM, FreemanBA. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem, 266:4244–4250. 1991.
283.
Ramos-GomezM, KwakMK, DolanPM, ItohK, YamamotoM, TalalayP, KenslerTW. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc Natl Acad Sci U S A, 98:3410–3415. 2001.
284.
RenX, BjörnstedtM, ShenB, EricsonML, HolmgrenA. Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione. Biochemistry, 32:9701–9708. 1993.
RheeSG. Cell signaling. H2O2, a necessary evil for cell signaling. Science, 312:1882–1883. 2006.
287.
RheeSG, ChangTS, BaeYS, LeeSR, KangSW. Cellular regulation by hydrogen peroxide. J Am Soc Nephrol, 14:S211–S215. 2003.
288.
RheeSG, WooHA. Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones. Antioxid Redox Signal, 15:781–794. 2011.
289.
RiemerJ, BulleidN, HerrmannJM. Disulfide formation in the ER and mitochondria: two solutions to a common process. Science, 324:1284–1287. 2009.
290.
RiemerJ, FischerM, HerrmannJM. Oxidation-driven protein import into mitochondria: insights and blind spots. Biochim Biophys Acta, 1808:981–989. 2011.
291.
RigobelloMP, Donella-DeanaA, CesaroL, BindoliA. Isolation, purification, and characterization of a rat liver mitochondrial protein disulfide isomerase. Free Radic Biol Med, 28:266–272. 2000.
292.
RigobelloMP, Donella-DeanaA, CesaroL, BindoliA. Distribution of protein disulphide isomerase in rat liver mitochondria. Biochem J, 356:567–570. 2001.
293.
RigobelloMP, FoldaA, BaldoinMC, ScutariG, BindoliA. Effect of auranofin on the mitochondrial generation of hydrogen peroxide. Role of thioredoxin reductase. Free Radic Res, 39:687–695. 2005.
294.
RigobelloMP, FoldaA, ScutariG, BindoliA. The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria. Arch Biochem Biophys, 441:112–122. 2005.
295.
RigobelloMP, ScutariG, BoscoloR, BindoliA. Induction of mitochondrial permeability transition by auranofin, a gold(I)-phosphine derivative. Br J Pharmacol, 136:1162–1168. 2002.
296.
RigobelloMP, ScutariG, FoldaA, BindoliA. Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c. Biochem Pharmacol, 67:689–696. 2004.
297.
RigobelloMP, TurcatoF, BindoliA. Inhibition of rat liver mitochondrial permeability transition by respiratory substrates. Arch Biochem Biophys, 319:225–230. 1995.
298.
RigouletM, YoboueED, DevinA. Mitochondrial ROS generation and its regulation: mechanisms involved in H2O2 signaling. Antioxid Redox Signal, 14:459–468. 2011.
299.
RinnaA, TorresM, FormanHJ. Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic Biol Med, 41:86–91. 2006.
300.
RoveriA, CasascoA, MaiorinoM, DalanP, CalligaroA, UrsiniF. Phospholipid hydroperoxide glutathione peroxidase of rat testis. Gonadotropin dependence and immunocytochemical identification. J Biol Chem, 267:6142–6146. 1992.
301.
RoyS, KhannaS, SenCK. Redox regulation of the VEGF signaling path and tissue vascularization: Hydrogen peroxide, the common link between physical exercise and cutaneous wound healing. Free Radic Biol Med, 44:180–192. 2008.
302.
RuoppoloM, Lundström-LjungJ, TalamoF, PucciP, MarinoG. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry, 36:12259–12267. 1997.
303.
SaggioroD, RigobelloMP, PaloschiL, FoldaA, MoggachSA, ParsonsS, RonconiL, FregonaD, BindoliA. Gold(III)-dithiocarbamato complexes induce cancer cell death triggered by thioredoxin redox system inhibition and activation of ERK pathway. Chem Biol, 14:1128–1139. 2007.
304.
SaitohM, NishitohH, FujiiM, TakedaK, TobiumeK, SawadaY, KawabataM, MiyazonoK, IchijoH. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J, 17:2596–2606. 1998.
305.
SakonS, XueX, TakekawaM, SasazukiT, OkazakiT, KojimaY, PiaoJH, YagitaH, OkumuraK, DoiT, NakanoH. NF-κB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death. EMBO J, 22:3898–3909. 2003.
306.
SalmeenA, AndersenJN, MyersMP, MengTC, HinksJA, TonksNK, BarfordD. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature, 423:769–773. 2003.
307.
SangS, LambertJD, HongJ, TianS, LeeMJ, StarkRE, HoCT, YangCS. Synthesis and structure identification of thiol conjugates of (-)-epigallocatechin gallate and their urinary levels in mice. Chem Res Toxicol, 18:1762–1769. 2005.
ScarbroughPM, MapuskarKA, MattsonDM, GiusD, WatsonWH, SpitzDR. Simultaneous inhibition of glutathione- and thioredoxin-dependent metabolism is necessary to potentiate 17AAG-induced cancer cell killing via oxidative stress. Free Radic Biol Med, 52:436–443. 2012.
310.
SchönbrunnerER, MayerS, TropschugM, FischerG, TakahashiN, SchmidFX. Catalysis of protein folding by cyclophilins from different species. J Biol Chem, 266:3630–3635. 1991.
311.
SchreckR, RieberP, BaeuerlePA. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J, 10:2247–2258. 1991.
SemenzaGL. Hypoxia-inducible factors in physiology and medicine. Cell, 148:399–408. 2012.
314.
SenCK. Cellular thiols and redox-regulated signal transduction. Curr Top Cell Regul, 36:1–30. 2000.
315.
SenguptaR, HolmgrenA. The role of thioredoxin in the regulation of cellular processes by S-nitrosylation. Biochim Biophys Acta, 1820:689–700. 2012.
316.
SerranderL, CartierL, BedardK, BanfiB, LardyB, PlastreO, SienkiewiczA, FórróL, SchlegelW, KrauseKH. NOX4 activity is determined by mRNA levels and reveals a unique pattern of ROS generation. Biochem J, 406:105–114. 2007.
317.
SevierCS, KaiserCA. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol, 3:836–847. 2002.
318.
SevierCS, KaiserCA. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta, 1783:549–556. 2008.
319.
SiesH. Oxidative stress: Introductory remarks. Oxidative stress. SiesH. London, Orlando, San Diego, New York, Toronto, Montreal, Sydney, Tokyo: Academic Press, 1985; 1–8.
320.
SiliprandiN, SiliprandiD, BindoliA, ToninelloA. Effect of oxidation of glutathione and membrane thiol groups on mitochondrial functions. Functions of Glutathione in Liver and Kidney. SiesH, WendelA. Berlin, Heidelberg: Springer-Verlag, 1978; 139–147.
321.
SmythiesJ. Does the O'Brien cycle occur in vivo as a key component in H2O2 production and redox signalling?Med Hypotheses, 76:299–301. 2011.
322.
SohnJ, RudolphJ. Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. Biochemistry, 42:10060–10070. 2003.
323.
SongJJ, LeeYJ. Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1. Biochem J, 373:845–853. 2003.
324.
Sousa-LopesA, AntunesF, CyrneL, MarinhoHS. Decreased cellular permeability to H2O2 protects Saccharomyces cerevisiae cells in stationary phase against oxidative stress. FEBS Lett, 578:152–156. 2004.
325.
St-PierreJ, BuckinghamJA, RoebuckSJ, BrandMD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem, 277:44784–44790. 2002.
326.
StaalFJ, RoedererM, HerzenbergLA, HerzenbergLA. Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus. Proc Natl Acad Sci U S A, 87:9943–9947. 1990.
StewartEJ, ÅslundF, BeckwithJ. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J, 17:5543–5550. 1998.
331.
StoneJR. An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys, 422:119–124. 2004.
StorzG, TartagliaLA. OxyR: a regulator of antioxidant genes. J Nutr, 122:627–630. 1992.
334.
SundaresanM, YuZX, FerransVJ, IraniK, FinkelT. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science, 270:296–299. 1995.
335.
SurhYJ, KunduJK, NaHK. Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals. Planta Medica, 74:1526–1539. 2008.
TannerJJ, ParsonsZD, CummingsAH, ZhouH, GatesKS. Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid Redox Signal, 15:77–97. 2011.
338.
TavenderTJ, BulleidNJ. Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid Redox Signal, 13:1177–1187. 2010.
339.
TavenderTJ, BulleidNJ. Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation. J Cell Sci, 123:2672–2679. 2010.
340.
TavenderTJ, SpringateJJ, BulleidNJ. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J, 29:4185–4197. 2010.
341.
TerentyevD, GyörkeI, BelevychAE, TerentyevaR, SridharA, NishijimaY, de BlancoEC, KhannaS, SenCK, CardounelAJ, CarnesCA, GyörkeS. Redox modification of ryanodine receptors contributes to sarcoplasmic reticulum Ca2+ leak in chronic heart failure. Circ Res, 103:1466–1472. 2008.
342.
ThannickalVJ, FanburgBL. Reactive oxygen species in cell signaling. Am J Physiol Lung Cell Mol Physiol, 279:L1005–L1028. 2000.
343.
TkachevVO, MenshchikovaEB, ZenkovNK. Mechanism of the Nrf2/Keap1/ARE signaling system. Biochemistry (Moscow), 76:407–422. 2011.
344.
TongKI, KobayashiA, KatsuokaF, YamamotoM. Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol Chem, 387:1311–1320. 2006.
345.
TonissenKF, Di TrapaniG. Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy. Mol Nutr Food Res, 53:87–103. 2009.
346.
TonksNK. Redox redux: revisiting PTPs and the control of cell signaling. Cell, 121:667–670. 2005.
347.
ToppoS, FlohéL, UrsiniF, VaninS, MaiorinoM. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim Biophys Acta, 1790:1486–1500. 2009.
348.
TretterL, Adam-ViziV. Generation of reactive oxygen species in the reaction catalyzed by α-ketoglutarate dehydrogenase. J Neurosci, 24:7771–7778. 2004.
349.
TrotterEW, GrantCM. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep, 4:184–188. 2003.
350.
TrujilloM, RadiR. Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: new insights into the reaction of peroxynitrite with thiols. Arch Biochem Biophys, 397:91–98. 2002.
351.
TuBP, WeissmanJS. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol, 164:341–346. 2004.
UrigS, BeckerK. On the potential of thioredoxin reductase inhibitors for cancer therapy. Semin Cancer Biol, 16:452–465. 2006.
354.
UrsiniF, HeimS, KiessM, MaiorinoM, RoveriA, WissingJ, FlohéL. Dual function of the selenoprotein PHGPx during sperm maturation. Science, 285:1393–1396. 1999.
355.
van der VlietA. NADPH oxidases in lung biology and pathology: Host defense enzymes, and more. Free Radic Biol Med, 44:938–955. 2008.
356.
van MontfortRLM, CongreveM, TisiD, CarrR, JhotiH. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature, 423:773–777. 2003.
357.
VepaS, ScribnerWM, NatarajanV. Activation of protein phosphorylation by oxidants in vascular endothelial cells: identification of tyrosine phosphorylation of caveolin. Free Radic Biol Med, 22:25–35. 1997.
358.
VignaisPV. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci, 59:1428–1459. 2002.
359.
WakabayashiN, Dinkova-KostovaAT, HoltzclawWD, KangMI, KobayashiA, YamamotoM, KenslerTW, TalalayP. Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers. Proc Natl Acad Sci U S A, 101:2040–2045. 2004.
360.
WelshSJ, BellamyWT, BriehlMM, PowisG. The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1α protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis. Cancer Res, 62:5089–5095. 2002.
361.
WilkinsonB, GilbertHF. Protein disulfide isomerase. Biochim Biophys Acta, 1699:35–44. 2004.
362.
WinterbournCC. Reconciling the chemistry and biology of reactive oxygen species. Nat Chem Biol, 4:278–286. 2008.
363.
WinterbournCC, HamptonMB. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med, 45:549–561. 2008.
364.
WinterbournCC, MetodiewaD. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med, 27:322–328. 1999.
365.
WooHA, ChaeHZ, HwangSC, YangKS, KangSW, KimK, RheeSG. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science, 300:653–656. 2003.
366.
WoodZA, PooleLB, KarplusPA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science, 300:650–653. 2003.
367.
WoodZA, SchroderE, Robin HarrisJ, PooleLB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci, 28:32–40. 2003.
368.
YangKS, KangSW, WooHA, HwangSC, ChaeHZ, KimK, RheeSG. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J Biol Chem, 277:38029–38036. 2002.
369.
YehJI, ClaiborneA, HolWGJ. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 Å resolution. Biochemistry, 35:9951–9957. 1996.
370.
YingJ, SharovV, XuS, JiangB, GerrityR, SchöneichC, CohenRA. Cysteine-674 oxidation and degradation of sarcoplasmic reticulum Ca2+ ATPase in diabetic pig aorta. Free Radic Biol Med, 45:756–762. 2008.
371.
ZhangDD, HanninkM. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol, 23:8137–8151. 2003.
372.
ZhangDX, GuttermanDD. Mitochondrial reactive oxygen species-mediated signaling in endothelial cells. Am J Physiol Heart Circ Physiol, 292:H2023–H2031. 2007.
373.
ZhangH, GoYM, JonesDP. Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch Biochem Biophys, 465:119–126. 2007.
374.
ZhangR, Al-LamkiR, BaiL, StrebJW, MianoJM, BradleyJ, MinW. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res, 94:1483–1491. 2004.
375.
ZhangZY, DixonJE. Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402. Biochemistry, 32:9340–9345. 1993.
376.
ZhengM, ÅslundF, StorzG. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science, 279:1718–1721. 1998.
377.
ZhouHY, SinghH, ParsonsZD, LewisSM, BhattacharyaS, SeinerDR, LaButtiJN, ReillyTJ, TannerJJ, GatesKS. The biological buffer bicarbonate/CO2potentiates H2O2-mediated inactivation of protein tyrosine phosphatases. JAm Chem Soc, 133:15803–15805. 2011.
378.
ZinkevichNS, GuttermanDD. ROS-induced ROS release in vascular biology: redox-redox signaling. Am J Physiol Heart Circ Physiol, 301:H647–H653. 2011.
379.
ZitoE, MeloEP, YangY, WahlanderA, NeubertTA, RonD. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell, 40:787–797. 2010.
380.
ZoccaratoF, CavalliniL, AlexandreA. Respiration-dependent removal of exogenous H2O2 in brain mitochondria. Inhibition by Ca2+J Biol Chem, 279:4166–4174. 2004.